Protein Products and Methods for Making the Same

ABSTRACT

According to one embodiment, a protein product may include a mixture of water and particulate matter comprising protein. The mixture may include medium chain aldehydes and pyrazines. The ratio of a total concentration of medium chain aldehydes in the mixture to a total concentration of pyrazines in the mixture, as determined by gas chromatography-mass spectrometry, may be greater than or equal to 0.5 and less than or equal to 45. The mixture may also include from about 0.5 wt. % to about 8.0 wt. % total protein by weight of the mixture. In addition, the mixture may include from about 40 wt. % to about 98 wt. % water by weight of the mixture and less than or equal to about 4.0 wt. % oil and fat by weight of the mixture. The particulate matter may have an average particle size less than or equal to about 50 μm.

CROSS REFERENCE TO RELATED APPLICATIONS

The present specification claims priority to U.S. patent applicationSer. No. 15/069,218 filed Mar. 14, 2016 and entitled “PROTEIN PRODUCTSAND METHODS FOR MAKING THE SAME,” the entirety of which is incorporatedby referenced herein.

BACKGROUND ART

The present specification generally relates to protein products and,more specifically, to beverage products containing protein from aplant-based protein source and methods for making the same.

TECHNICAL FIELD

A common and relatively inexpensive source of protein is dairy products,specifically dairy milk. However, there is a concern over the exposureof milk cows to antibiotics, hormones, and genetically modifiedsubstances (i.e., plant material used as livestock feed) and thepossibility that such substances may be passed to the consumer throughdairy milk. In addition, some consumers are lactose intolerant makingdairy milk difficult to consume while still others find the caloriccontent and/or cholesterol content of dairy milk to be relatively high,particularly those consumers on restricted diets. As such, there isgrowing demand for a healthy, good tasting source of protein that may beused as a replacement for dairy milk.

Several alternatives to dairy milk are available on the market today.These alternatives include, for example, almond milk, cashew milk, andsoy milk. While popular amongst consumers, each of these products hasdrawbacks. For example, milk substitutes derived from almonds andcashews have a low protein content relative to dairy milk. The dairymilk industry has keyed on this property and current ad copy touts therelatively high protein content in dairy milk versus the low proteincontent in milk substitutes derived from almonds and/or cashews.Further, milk substitutes derived from soy may contain phytoestrogensand protease inhibitors from soy, which some consumers find undesirable.Moreover, soy plants from which the soy milk is derived are agenetically modified organism (GMO) which some consumers may also findundesirable.

Accordingly, a need exists for an alternative substitute for dairy milkwhich is plant-based, cholesterol-free, lactose free, and relatively lowcalorie, but which also has high protein content.

SUMMARY OF INVENTION

According to one embodiment, a protein product may include a mixture ofwater and particulate matter comprising protein. The mixture may includemedium chain aldehydes and pyrazines. The ratio of a total concentrationof medium chain aldehydes in the mixture to a total concentration ofpyrazines in the mixture, as determined by gas chromatography-massspectrometry, may be greater than or equal to 0.5 and less than or equalto 45. The mixture may also include from about 0.5 wt. % to about 8.0wt. % total protein by weight of the mixture. In addition, the mixturemay include from about 40 wt. % to about 98 wt. % water by weight of themixture and less than or equal to about 4.0 wt. % oil and fat by weightof the mixture. The particulate matter may have an average particle sizeless than or equal to about 50 μm.

In another embodiment, a protein product may include a mixture of waterand particulate matter comprising protein aggregates derived frompeanuts. The protein aggregates may have an average aggregate size ofgreater than or equal to 4 microns. The mixture may also include fromabout 0.5 wt. % to about 8.0 wt. % total protein by weight of themixture, from about 40 wt. % to about 98 wt. % water by weight of themixture; and less than or equal to about 4.0 wt. % oil and fat by weightof the mixture.

In another embodiment, a method of making a protein product may includeprocessing nuts with a heat load greater than or equal to 3, wherein thenuts are at least one of tree nuts and peanuts. The nuts may be groundthereby forming a protein paste. The protein paste may be blended withwater thereby forming a mixture having a total protein content fromabout 0.5 wt. % to about 8.0 wt. % by weight of the mixture. The oil andfat content of the mixture may be reduced to less than or equal to about4.0 wt. % by weight of the mixture. Thereafter, the mixture may besterilized with an indirect sterilization process whereby, aftersterilization, the mixture comprises protein aggregates having anaverage aggregate size greater than or equal to 4 microns.

Additional features and advantages of the protein products describedherein and methods for making the same will be set forth in the detaileddescription which follows, and will be readily apparent to those skilledin the art from that description or recognized by practicing theembodiments described herein, including the detailed description whichfollows, the claims, as well as the appended drawings.

It is to be understood that both the foregoing general description andthe following detailed description describe various embodiments and areintended to provide an overview or framework for understanding thenature and character of the claimed subject matter. The accompanyingdrawings are included to provide a further understanding of the variousembodiments, and are incorporated into and constitute a part of thisspecification. The drawings illustrate the various embodiments describedherein, and together with the description serve to explain theprinciples and operations of the claimed subject matter.

BRIEF DESCRIPTION OF DRAWINGS

FIG. 1 schematically depicts an indirect sterilization process accordingto one or more embodiments shown and described herein;

FIG. 2 schematically depicts another indirect sterilization processaccording to one or more embodiments shown and described herein;

FIG. 3 graphically depicts the ratio of medium chain aldehydes topyrazines as a function of heat load;

FIG. 4 graphically depicts the ratio of medium chain aldehydes topyrazines as a function of processing conditions;

FIG. 5 graphically depicts the relative amount of the medium chainaldehyde hexanal as a function of processing conditions;

FIG. 6 graphically depicts the relative amount of the pyrazine compoundmethylpyrazine as a function of processing conditions;

FIG. 7 graphically depicts the relative amount of the pyrazine compoundtrimethylpyrazine as a function of processing conditions;

FIG. 8 is a magnified image of a peanut milk sample prior tosterilization showing the degree of protein aggregation in the sample;

FIG. 9 is a magnified image of a peanut milk sample after exposure to adirect sterilization process showing the degree of protein aggregationin the sample as a result of the direct sterilization process;

FIG. 10 is a magnified image of a peanut milk sample after exposure toan indirect sterilization process showing the degree of proteinaggregation in the sample as a result of the indirect sterilizationprocess; and

FIG. 11 is a magnified image of a peanut milk sample after exposure toan indirect sterilization process showing the degree of proteinaggregation in the sample as a result of the indirect sterilizationprocess.

DETAILED DESCRIPTION

Reference will now be made in detail to various embodiments of proteinproducts, such as beverages, and methods for making the same. Wheneverpossible, the same reference numerals will be used throughout thedrawings to refer to the same or like parts. According to embodiments, aprotein product, such as a beverage, may include a mixture of water andparticulate matter comprising protein. The particulate matter may havean average particle size less than or equal to about 50 μm. The mixturemay include medium chain aldehydes and pyrazines. A ratio of a totalconcentration of medium chain aldehydes in the mixture to a totalconcentration of pyrazines in the mixture, as determined by gaschromatography-mass spectrometry, may be greater than or equal to 1 andless than or equal to 30. The mixture may further include from about 0.5wt. % to about 8.0 wt. % total protein by weight of the mixture and fromabout 70 wt. % to about 98 wt. % water by weight of the mixture. Themixture may further include less than or equal to about 4.0 wt. % oiland fat by weight of the mixture. Various embodiments of proteinproducts and methods for making the same will be described in furtherdetail herein with specific reference to the appended drawings.

It should be understood that, unless otherwise specified, terms such as“top,” “bottom,” “outward,” “inward,” and the like are words ofconvenience and are not to be construed as limiting terms. In addition,whenever a group is described as comprising at least one of a group ofelements and combinations thereof, it is understood that the group maycomprise, consist essentially of, or consist of any number of thoseelements recited, either individually or in combination with each other.Similarly, whenever a group is described as consisting of at least oneof a group of elements or combinations thereof, it is understood thatthe group may consist of any number of those elements recited, eitherindividually or in combination with each other.

Unless otherwise specified, a range of values, when recited, includesboth the upper and lower limits of the range as well as any rangestherebetween. As used herein, the indefinite articles “a,” “an,” and thecorresponding definite article “the” mean “at least one” or “one ormore,” unless otherwise specified. It also is understood that thevarious features disclosed in the specification and the drawings can beused in any and all combinations.

Tree nuts and legumes, such as peanuts and soy beans, contain proteinand may be used as a basis for dairy milk substitutes. One drawback tousing tree nuts and legumes as a basis for dairy milk substitutes is thepresence of (or potential to develop) organic aroma compounds which, inturn, may impart an undesirable or “off” flavor in the resulting productat certain levels. Specifically, volatile organic aroma compounds, suchas pyrazines and medium chain aldehydes, may be present in the raw treenuts and legumes and/or may develop during processing of the tree nutsand legumes into a protein-containing product such as a dairy milksubstitute. These organic aroma compounds may have a very low sensorydetection threshold and, as a result, can strongly influence the flavorof the resulting product. For example, when raw or unprocessed, sometree nuts and legumes may contain medium chain aldehydes, such ashexanal or the like. These organic aroma compounds may impart a “grassy”or “beany” flavor to the protein product which may be unacceptable tothe consumer at certain levels. Similarly, during processing, some treenuts and legumes may develop one or more pyrazine compounds which imparta strong roasted flavor which may be similarly unacceptable to theconsumer at certain levels. The methods for making protein productsdescribed herein provide a protein product, such as a dairy milksubstitute, in which the development of “off” flavors due to organicaroma compounds is mitigated.

In the embodiments described herein, the protein products may bebeverages for human consumption. The protein products may contain amixture of water and particulate matter which includes, among otherconstituents, protein. The particulate matter is derived from aplant-based protein source such as, for example, tree nuts, legumes,grains, vegetable proteins, or combinations thereof (referred tohereinafter as “the protein source”). Suitable tree nuts may include,without limitation, cashews and almonds. Suitable legumes may include,without limitation, soy beans and peanuts. Suitable grains may include,without limitation, oats, wheat, and quinoa. Suitable vegetable proteinsmay include, without limitation, pea protein. In some embodiments, theprotein products are made from peanuts and one or more tree nuts and/orsoy beans. In other embodiments, the protein products are made frompeanuts without the addition of tree nuts or other legumes. The relativeconcentrations of water and particulate matter may be adjusted to imparta desired consistency and/or viscosity to the protein product. Forexample, the concentration of water in the protein product may bedecreased to provide a beverage with the consistency or viscosity of a“shake” or a “smoothie.” Alternatively, the concentration of water inthe protein product may be increased to provide a beverage with aconsistency and/or viscosity similar to dairy milk.

In the embodiments described herein, the protein products may be made byfirst (and optionally) washing the raw protein source to remove anyremnants of dirt and/or organic debris, such as skins and the like. Forexample, the raw protein source may be rinsed in water having atemperature from about 10° C. to about 20° C. In embodiments where theprotein product comprises peanuts, the peanuts may contain, for example,from about 10 wt. % to about 15 wt. % water after the washing step.

In some embodiments, the protein source is optionally sterilized afterwashing or instead of washing. For example, in some embodiments theprotein source may be steam sterilized or steam pasteurized afterwashing or instead of washing to mitigate or eliminate any microbialload within the protein source. In embodiments, the optionalsterilization may be steam pasteurization at a temperature ofapproximately 220° F. (104.4° C.) for a time of approximately 20minutes.

After the optional washing step, the protein source is furtherprocessed, such as by heating, to mitigate off-flavors due to volatileorganic aroma compounds. This heating step may also reduce the microbialload within the protein source. For example, where the protein sourceincludes peanuts, the raw peanuts may contain medium chain aldehydes(i.e., aldehydes with C6-C10 carbon chains), such as hexanal or thelike, and which may impart a grassy or beany flavor to the raw peanuts.It has been found that heating the protein source may mitigate the offflavors imparted by the medium chain aldehydes by volatilizing theorganic aroma compounds, effectively driving the compounds from thepeanuts. However, it has also been found that heating the protein sourcemay promote the development of other volatile organic aroma compounds,such as pyrazines and the like, which may further contribute an offflavor to the protein source. For example, where the protein sourceincludes peanuts, roasting the peanuts for extended periods of timeand/or at higher temperatures causes pyrazine compounds to develop whichimpart a strong, roasted flavor to the peanuts. This roasted flavor isundesirable in a dairy milk substitute. Accordingly, in the embodimentsdescribed herein, the protein source is processed under conditions whichreduce the volatile organic aroma compounds in the raw protein source(such as medium chain aldehydes) while mitigating and/or eliminating thedevelopment of additional volatile organic aroma compounds (such aspyrazines).

In the embodiments described herein, it has been determined that certainratios of the total concentration of medium chain aldehydes in theprotein source to the total concentration of pyrazines in the proteinsource, as determined by gas chromatography-mass spectrometry, reduceand/or mitigate the occurrence of off flavors in the resultant proteinproduct. In the embodiments described herein, following processing byheating, the ratio of the total concentration of medium chain aldehydesin the protein source to the total concentration of pyrazines in theprotein source is greater than or equal to about 0.5 and less than orequal to about 45. It has been found that when the ratio is less thanabout 0.5, the resulting protein product will have an undesirableroasted or burnt flavor. However, when the ratio is greater than about45, the resulting protein product will have an undesirable “grassy” or“beany” flavor. In some embodiments, following processing by heating,the ratio of the total concentration of medium chain aldehydes in theprotein source to the total concentration of pyrazines in the proteinsource is greater than or equal to about 0.5 and less than or equal toabout 20. In some embodiments, following processing by heating, theratio of the total concentration of medium chain aldehydes in theprotein source to the total concentration of pyrazines in the proteinsource is greater than or equal to about 0.75 and less than or equal toabout 10. In some other embodiments, following processing by heating,the ratio of the total concentration of medium chain aldehydes in theprotein source to the total concentration of pyrazines in the proteinsource is greater than or equal to about 1 and less than or equal toabout 5. Analytical methods for determining the ratio of the totalconcentration of medium chain aldehydes to the total concentration ofpyrazines will be described in further detail in Example 1, below.

The specified ratios of the total concentration of medium chainaldehydes in the protein source to the total concentration of pyrazinesmay be obtained by processing the protein source within a certain rangeof applied heat loads. For a given temperature and heating time, theheat load F₀ is the equivalent exposure time to a temperature of 122.11°C. More specifically, the heat load F₀ is defined as:

${F_{0} = {\Delta \; t\; {\sum\; 10^{\frac{({T - 121})}{z}}}}}\;$

where:

-   -   T is the temperature of the protein source at time t;    -   Δt is the time interval between measurements of the temperature        T; and    -   z is the temperature coefficient, assumed to be 10° C.

In the embodiments described herein, the desired ratio of the totalconcentration of medium chain aldehydes in the protein source to thetotal concentration of pyrazines in the protein source may be achievedby processing the protein source under a heat load greater than or equalto about 3. For example, in some embodiments, the protein source may beprocessed under a heat load greater than or equal to about 3 and lessthan or equal to about 2000. In some embodiments, the protein source maybe processed under a heat load greater than or equal to about 15 andless than or equal to about 1800. In some other embodiments, the proteinsource may be processed under a heat load greater than or equal to about20 and less than or equal to about 1600. In still other embodiments, theprotein source may be processed under a heat load greater than or equalto about 25 and less than or equal to about 1400. In yet otherembodiments, the protein source may be processed under a heat loadgreater than or equal to about 30 and less than or equal to about 1200.In some other embodiments, the protein source may be processed under aheat load greater than or equal to about 35 and less than or equal toabout 1000. In some other embodiments, the protein source may beprocessed under a heat load greater than or equal to about 3 and lessthan or equal to about 500. In some embodiments, the protein source maybe processed under a heat load greater than or equal to about 15 andless than or equal to about 250. In some other embodiments, the proteinsource may be processed under a heat load greater than or equal to about20 and less than or equal to about 125. In still other embodiments, theprotein source may be processed under a heat load greater than or equalto about 25 and less than or equal to about 80. In yet otherembodiments, the protein source may be processed under a heat loadgreater than or equal to about 30 and less than or equal to about 60. Insome other embodiments, the protein source may be processed under a heatload greater than or equal to about 35 and less than or equal to about50.

In embodiments, the aforementioned heat loads are achieved by heatingthe protein source in air at a processing temperature greater than orequal to about 238° F. (114.4° C.) and less than or equal to about 310°F. (154.4° C.). In some other embodiments, the processing temperaturemay be greater than or equal to about 250° F. (121.1° C.) and less thanor equal to about 300° F. (148.8° C.). In still other embodiments, theprocessing temperature may be greater than or equal to about 250° F.(121.1° C.) and less than or equal to about 290° F. (154.4° C.). Instill other embodiments, the processing temperature may be greater thanor equal to about 250° F. (121.1° C.) and less than or equal to about285° F. (140.6° C.). In still other embodiments, the processingtemperature may be greater than or equal to about 250° F. (121.1° C.)and less than or equal to about 310° F. (154.4° C.). In still otherembodiments, the processing temperature may be greater than or equal toabout 255° F. (123.9° C.) and less than or equal to about 310° F.(154.4° C.). In still other embodiments, the processing temperature maybe greater than or equal to about 265° F. (129.4° C.) and less than orequal to about 310° F. (154.4° C.). In still other embodiments, theprocessing temperature may be greater than or equal to about 275° F.(135° C.) and less than or equal to about 310° F. (154.4° C.). In stillother embodiments, the processing temperature may be greater than orequal to about 280° F. (137.8° C.) and less than or equal to 3 about 10°F. (154.4° C.).

The protein source may be processed at the processing temperature for aprocessing time sufficient for the tree nuts to be subjected to thespecified heat load. In embodiments, the processing time is greater thanor equal to about 10 minutes and less than or equal to about 120minutes. In some other embodiments, the processing time is greater thanor equal to about 10 minutes and less than or equal to about 60 minutes.In still other embodiments, the processing time is greater than or equalto about 15 minutes and less than or equal to about 40 minutes. In yetother embodiments, the processing time is greater than or equal to about15 minutes and less than or equal to about 35 minutes.

In embodiments, a desired heat load may be achieved by processing theprotein source at, for example, about 238° F. (114.4° C.) for about 15minutes. Alternatively, a desired heat load may be achieved byprocessing the protein source at, for example, about 255° F. (123.9° C.)for about 20 minutes or even about 265° F. (129.4° C.) for about 20minutes. In yet an alternative, a desired heat load may be achieved byprocessing the protein source at, for example, about 285° F. (140.6° C.)for 20 minutes or even about 310° F. (154.4° C.) for about 15 minutes.It should be understood that the foregoing temperature and timecombinations are for purposes of illustration only and that othercombinations of time and temperature may suitable for obtaining a heatload greater than or equal to about 3 and less than or equal to about200 as described herein.

While processing the protein source at elevated temperatures reduces theoff flavors associated volatile organic aroma compounds, it also reducesthe water content of the protein source which, in turn, alters themechanical properties of the protein source, making it easier to obtaina desired particle size distribution in subsequent grinding operations.For example, in embodiments where the protein source include peanuts,the peanuts may have a moisture content greater than or equal to about0.5 wt. % and less than or equal to about 4 wt. % water by weight of theprotein source after heating. The reduction in moisture from, forexample, about 10 wt. % or greater by weight makes the peanuts morebrittle and more readily fractured into smaller component parts in asubsequent grinding operation. In embodiments, after processing atelevated temperatures, the protein source has a moisture content greaterthan or equal to about 0.5 wt. % and less than or equal to about 3 wt. %by weight. In some other embodiments, after processing at elevatedtemperatures, the protein source has a moisture content greater than orequal to about 0.75 wt. % and less than or equal to about 2 wt. % byweight.

After processing at elevated temperatures, the protein source is groundto a protein paste which consists of particulate matter and the oil andfat from the protein source. It should be understood that theparticulate matter includes protein but may also include carbohydrates,fiber, and fat. In the embodiments described herein, the protein sourceis ground without the addition of any further processing aids or fluids(i.e., water, oil or the like). The protein source is ground such thatthe resultant protein paste includes particulate matter (i.e., tree nutand/or legume particles) with an average particle size of less than orequal to about 50 microns. For example, in some embodiments the averageparticle size of the particulate matter in the protein paste is lessthan or equal to about 45 microns or even less than or equal to about 40microns. In some embodiments, the average particle size of theparticulate matter in the protein paste is less than or equal to about35 microns or even less than or equal to about 30 microns. In stillother embodiments, the average particle size of the particulate matterin the protein paste is less than or equal to about 20 microns.Decreasing the average particle size of the protein paste to less thanabout 50 microns or even less than about 45 microns prevents thedetection of the individual particulates by the human tongue, providinga consumable product which does not have a perceived “gritty” texture.

After the protein source is ground to a protein paste, the protein pasteis combined with water and blended to form a mixture of protein pasteand water with particulate matter contributed to the mixture by theprotein paste suspended in the water. In the embodiments describedherein, the mixture of protein paste and water includes greater than orequal to about 0.5 wt. % and less than or equal to about 35 wt. %protein paste. For example, in some embodiments, the mixture of proteinpaste and water includes greater than or equal to about 5 wt. % and lessthan or equal to about 30 wt. % protein paste. In some otherembodiments, the mixture of protein paste and water includes greaterthan or equal to about 5 wt. % and less than or equal to about 25 wt. %protein paste. In some other embodiments, the mixture of protein pasteand water includes greater than or equal to about 5 wt. % and less thanor equal to about 20 wt. % protein paste. In still other embodiments,the mixture of protein paste and water includes greater than or equal toabout 5 wt. % and less than or equal to about 15 wt. % protein paste.

In embodiments, the ratio of protein paste to water in the mixture maybe from about 1:4 to about 1:9. For example, in embodiments, the ratioof protein paste to water in the mixture may be from about 1:5 to about1:8 or even from about 1:5 to about 1:7.

In some embodiments, the mixture of protein paste and water may beoptionally filtered to remove larger particulates which may bedetectable by the human tongue, thereby further reducing the averageparticle size of the mixture to less than about 50 microns. For example,in some embodiments, the mixture of protein paste and water may bepassed through a filter and/or sieve which passes particulate matterless than or equal to about 50 microns and traps the particulate mattergreater than about 50 microns. In some other embodiments, the mixture ofprotein paste and water may be passed through a filter and/or sievewhich passes particulate matter less than or equal to about 45 micronsand traps particulate matter greater than about 45 microns. In stillother embodiments, the mixture of protein paste and water may be passedthrough a filter and/or sieve which passes particulate matter less thanor equal to about 40 microns and traps particulate matter greater thanabout 40 microns. However, it should be understood that this filteringstep is optional and that, in other embodiments, the mixture of proteinpaste and water is not filtered.

Thereafter, excess oil/fat is removed from the mixture. Specifically,the mixture of protein paste and water may be heated in a separator,such as a cream separator, centrifuge or the like, to at least partiallyremove the oil/fat from the mixture. In embodiments, the mixture ofprotein paste and water is heated to a temperature from about 122° F.(50° C.) to about 194° F. (90° C.) prior to being introduced into theseparator or while resident in the separator. After being passed throughthe separator, the mixture contains less than or equal to about 4.0 wt.% oil and fat by weight of the mixture or even less than or equal toabout 3.0 wt. % oil and fat by weight of the mixture. For example, insome embodiments, the mixture may contain greater than or equal to about0.5 wt. % and less than or equal to about 4.0 wt. % oil and fat byweight of the mixture after being passed through the separator. In someother embodiments, the mixture may contain greater than or equal toabout 0.5 wt. % and less than or equal to about 3.0 wt. % oil and fat byweight of the mixture after being passed through the separator. In someother embodiments, the mixture may contain greater than or equal toabout 1.0 wt. % and less than or equal to about 2.0 wt. % oil and fat byweight of the mixture after being passed through the separator.

After the oil and fat is separated from the remainder of the mixture,the mixture may be homogenized at elevated temperatures and pressuresand sterilized. In some embodiments, the mixture is first homogenizedand then sterilized while, in some other embodiments, the mixture ishomogenized as part of the sterilization process or homogenized afterthe sterilization process.

Homogenization aids in reducing the size of oil/fat particles in themixture and also prevents aggregation of particles in the mixture. Inembodiments, the mixture may be homogenized at temperatures greater thanor equal to about 158° F. (70° C.) or even greater than or equal toabout 167° F. (75° C.). In embodiments, the mixture may be homogenizedat pressures greater than or equal to about 3000 psi or even greaterthan or equal to about 5000 psi. In some embodiments the mixture may behomogenized in consecutive steps in which the pressure is increasedduring each consecutive step. For example, in some embodiments, themixture may be homogenized in a two step process in which thetemperature is greater than or equal to about 158° F. (70° C.) and thepressure is about 3000 psi in the first step and the temperature isgreater than or equal to about 158° F. (70° C.) and the pressure isabout 5000 psi in the second step.

In the embodiments described herein, sterilization may be doneindirectly, without co-mingling the sterilization utility (e.g., steam,hot water, etc.) with the mixture. It has been unexpectedly found thatthe use of indirect sterilization provides for a desirable aggregationof the proteins in the mixture, increasing the protein size andimproving the mouth feel and texture of the product. In embodiments, themixture may be sterilized, for example, by indirect tube and shellsterilization or, alternatively, indirect scrape surface sterilization,each of which are described in further detail below.

Referring now to FIG. 1, an indirect tube and shell sterilizationprocess 100 is schematically depicted. In this sterilization process,the mixture may be initially heated from approximately 45° F. (7.2° C.)to approximately 185° F. (85° C.) or even 240° F. (115.6° C.) in apre-heater 102. In embodiments, the pre-heater 102 may be, for example,a plate-frame heat exchanger which isolates the mixture from the heatingutility. Thereafter, the mixture is passed to a homogenizer 104 wherethe mixture is homogenized. In embodiments, the mixture may behomogenized at, for example, a temperature of 185° F. and a pressure of3500 psi.

The mixture is then passed to a tubular heater 106 where the mixture isheated and sterilized. In embodiments, the tubular heater 106 comprisesa tube-in-shell design in which the mixture being sterilized is carriedwithin an inner tube and the heating utility, such as steam and/orwater, is carried in a space between the inner tube and a shellsurrounding the inner tube such that the heating utility and the mixtureare isolated from one another (i.e., the heating utility and the mixtureare not co-mingled). In embodiments, the heating utility is provided ata temperature suitable to heat the mixture to a sterilizationtemperature from greater than or equal to about 265° F. (129.4° C.) toless than or equal to about 285° F. (140.6° C.) and held at thesterilization temperature for a time period from greater than or equalto about 5 seconds to less than or equal to about 15 seconds in order tosterilize the mixture. In embodiments, the mixture is held at 275° F.(135° C.) for a holding period of 7 seconds in order to complete thesterilization process.

After sterilization in the tubular heater 106, the mixture is passed toa cooler where the mixture is cooled. In embodiments, the cooler may bea tubular cooler 108 as depicted in FIG. 1. The tubular cooler 108comprises a tube-in-shell design in which the mixture is carried withinan inner tube and the cooling utility, such as water or a coolant, iscarried in a space between the inner tube and a shell surrounding theinner tube such that the cooling utility and the mixture are isolatedfrom one another (i.e., the cooling utility and the mixture are notco-mingled). While FIG. 1 depicts the use of a tubular cooler 108, itshould be understood that other types of coolers and/or combinations ofcoolers are contemplated and possible. In embodiments, the coolingutility may be provided at a temperature suitable to cool the mixture toa temperature of, for example, approximately 45° F. (7.2° C.).

In another embodiment, the mixture may be sterilized in an indirectscrape surface process as depicted in FIG. 2. Like the indirect tube andshell process 100 of FIG. 1, the indirect scrape surface process 150 ofFIG. 2 prevents the co-mingling of the heating utility and the mixture,thereby allowing for the aggregation of proteins in the mixture. Inembodiments, the indirect scrape surface process 150 may includeinitially homogenizing the mixture in a homogenizer 152. In embodiments,the mixture may be homogenized at, for example, a temperature ofapproximately 165° F. (74° C.) and a pressure of 3500 psi.

Thereafter, the mixture is passed to a pre-heater 154 where the mixtureis heated from the homogenization temperature to a temperature within arange from greater than or equal to about 165° F. (74° C.) to less thanor equal to about 240° F. (115.6° C.). In embodiments, the mixture maybe heated in the pre-heater 154 to a temperature within a range fromgreater than or equal to about 185° F. (85° C.) to less than or equal toabout 200° F. (93.3° C.). In embodiments, the pre-heater 154 may be, forexample, a plate-frame heat exchanger which isolates the mixture fromthe heating utility.

Thereafter, the mixture is passed from the pre-heater 154 to a scrapesurface heater 156 where the mixture is heated to a sterilizationtemperature from greater than or equal to about 265° F. (129.4° C.) toless than or equal to about 285° F. (140.6° C.). The mixture is exposedto the sterilization temperature for a time period from greater than orequal to about 5 seconds to less than or equal to about 15 seconds inorder to sterilize the mixture. The scrape surface heater generallycomprises a vessel which includes a rotating stirrer engaged with thesidewalls of the vessel to agitate product within the vessel. The vesselfurther includes an outer shell or coils through which a heating utilityis circulated to heat the product within the vessel without co-minglingthe heating utility and the product. The mixture is introduced into thescrape surface heater 156 proximate the bottom of the vessel, heatedwithin the vessel, and the heated mixture is extracted from the vesselproximate the top of the vessel.

The mixture is then passed to a cooler 158 where the mixture is cooled.In embodiments, the mixture may exit the cooler at a temperature ofapproximately 45° F. (7.2° C.). In embodiments the cooler 158 mayinclude a pre-cooler 160 and a scrape surface cooler 162. The pre-cooler160 may be utilized to cool the mixture from approximately 275° F. (135°C.) to approximately 65° F. (18.3° C.) or even 60° F. (15.6° C.). Thepre-cooler 160 may be, for example, a plate-frame heat exchanger whichisolates the mixture from the cooling utility. Alternatively, thepre-cooler 160 may be a tubular cooler, as described above with respectto FIG. 1. In embodiments, the cooler 158 may further include a scrapesurface cooler 162. The scrape surface cooler 162 may further cool themixture to a temperature of approximately 45° C. upon exiting thepre-cooler 160. The scrape surface cooler 162 generally comprises avessel which includes a rotating stirrer engaged with the sidewalls ofthe vessel to agitate product within the vessel. The vessel furtherincludes an outer shell or coils through which a cooling utility, suchas water or coolant, is circulated to cool the product within the vesselwithout co-mingling the cooling utility and the product. The mixture isintroduced into the scrape surface cooler 162 proximate the top of thevessel, cooled within the vessel, and the cooled mixture is extractedfrom the vessel proximate the bottom of the vessel.

While FIG. 2 depicts the use of a cooler 158 which includes a pre-cooler160 and a scrape surface cooler 162, it should be understood that othertypes of coolers and/or combinations of coolers are contemplated andpossible.

While two methods of indirect sterilization have been described herein,it should be understood that other methods and processes arecontemplated and possible. Further, while specific ranges oftemperatures and times have been provided for various portions of theindirect sterilization methods of FIGS. 1 and 2, it should be understoodthat these temperatures and times are for purposes of illustration andthat variations in the temperature and/or times may be used to achievethe same results with respect to the aggregation of proteins in themixture.

As noted hereinabove, it has been unexpectedly found that the use ofindirect sterilization methods, such as the indirect tube and shellsterilization method and the indirect scrape surface sterilizationmethod, results in the aggregation of proteins in the mixture thatincreases the average protein aggregate size and provides a moredesirable mouth feel and texture to the mixture. These proteinaggregates may include, without limitation, protein, fat droplets, andstarch.

In the embodiments described herein, after sterilization, the mixturecomprises protein aggregates which have an average particle size ofgreater than or equal to about 4 microns. These protein aggregates aregenerally loose, low-density structures which contribute to the smoothtexture of the mixture in the mouth. In embodiments, the mixturecomprises protein aggregates which have an average aggregate particlesize of greater than or equal to about 4 microns and less than or equalto about 150 microns. In some embodiments, after sterilization, themixture comprises protein aggregates which have an average aggregateparticle size of greater than or equal to about 4 microns and less thanor equal to about 70 microns. In some other embodiments, aftersterilization, the mixture comprises protein aggregates which have anaverage aggregate particle size of greater than or equal to about 4microns and less than or equal to about 35 microns. In still otherembodiments, after sterilization, the mixture comprises proteinaggregates which have an average aggregate particle size of greater thanor equal to about 4 microns and less than or equal to about 15 microns.In some other embodiments, after sterilization, the mixture comprisesprotein aggregates which have an average aggregate particle size ofgreater than or equal to about 4 microns and less than or equal to about12 microns. In some other embodiments, after sterilization, the mixturecomprises protein aggregates which have an average aggregate particlesize of greater than or equal to about 4 microns and less than or equalto about 10 microns.

It should now be understood that the resultant protein product comprisesa mixture of water and particulate matter comprising protein which maybe consumed as a beverage, for example. The protein product may includeadditional additives including, without limitation, preservatives,colorants, sweeteners, and the like, in addition to the mixture. Asnoted hereinabove, the protein source which provide the protein contentto the beverage are processed to minimize the contribution of offflavors due to volatile organic aroma compounds from the protein source.While most of these volatile organic aroma compounds are eliminated ormitigated by processing the raw protein source at elevated temperaturesprior to forming the mixture, it is hypothesized that volatile organicaroma compounds may develop during subsequent processing steps, such asduring separation, homogenization and sterilization. Accordingly, ineach of these processing steps, the temperature of the mixture iscontrolled to mitigate the evolution of volatile organic aroma compoundswhich may alter the flavor of the protein product.

In the embodiments described herein, the mixture of water and proteinsource includes, after sterilization, medium chain aldehydes andpyrazines with a ratio of the total concentration of medium chainaldehydes in the mixture to a total concentration of pyrazines in themixture, as determined by gas chromatography-mass spectrometry, greaterthan or equal to about 0.5 and less than or equal to about 45. Inembodiments, the ratio of the total concentration of medium chainaldehydes in the mixture to a total concentration of pyrazines in themixture is greater than or equal to about 0.5 and less than or equal toabout 20. In still other embodiments, the ratio of the totalconcentration of medium chain aldehydes in the mixture to a totalconcentration of pyrazines in the mixture is greater than or equal toabout 0.75 and less than or equal to about 10. In yet other embodiments,the ratio of the total concentration of medium chain aldehydes in themixture to a total concentration of pyrazines in the mixture is greaterthan or equal to about 1 and less than or equal to about 5. Inembodiments, the ratio of the total concentration of medium chainaldehydes in the mixture to a total concentration of pyrazines in themixture, as determined by gas chromatography-mass spectrometry, isgreater than or equal to about 1, or even greater than or equal to about2, and less than or equal to about 45. In embodiments, the ratio of thetotal concentration of medium chain aldehydes in the mixture to a totalconcentration of pyrazines in the mixture is greater than or equal toabout 3 and less than or equal to about 45. In embodiments, the ratio ofthe total concentration of medium chain aldehydes in the mixture to atotal concentration of pyrazines in the mixture is greater than or equalto about 1, or even greater than or equal to about 2, and less than orequal to about 20. In embodiments, the ratio of the total concentrationof medium chain aldehydes in the mixture to a total concentration ofpyrazines in the mixture is greater than or equal to about 3 and lessthan or equal to about 20. In still other embodiments, the ratio of thetotal concentration of medium chain aldehydes in the mixture to a totalconcentration of pyrazines in the mixture is greater than or equal toabout 1, or even greater than or equal to about 2, and less than orequal to about 10. In still other embodiments, the ratio of the totalconcentration of medium chain aldehydes in the mixture to a totalconcentration of pyrazines in the mixture is greater than or equal toabout 3 and less than or equal to about 10. In yet other embodiments,the ratio of the total concentration of medium chain aldehydes in themixture to a total concentration of pyrazines in the mixture is greaterthan or equal to about 1 and less than or equal to about 5.

According to some embodiments, the mixture may further include pHbuffers in addition to water and the protein paste. The pH buffersprotect against separation of the protein from the water when themixture is added to an acidic environment, such as, for example, coffeeor tea. Without being bound to any particular theory, it is believedthat proteins generally stay in solution when they are positively ornegatively charged because they are attracted to oppositely chargedparticles of the solvent. For instance, a positively charged protein isattracted to negatively charged particles in the solvent, therebypreventing flocculation of the proteins and, ultimately, preventingsedimentation. However, it is believed that the isoelectric point of theproteins in the mixture is higher than the pH of beverages to which themixture is likely to be added, such as, for example, coffee and tea. Inthis case, when the mixture of protein paste and water is added to suchbeverages, the resulting solution may have a pH at or below theisoelectric point of the proteins. When this happens, the charge of theproteins in the mixture is approximately neutral and the proteins in themixture are not attracted to positively or negatively charged particlesin the solvent. Accordingly, when the proteins are in a system with a pHat or below their isoelectric point, the proteins are less likely tostay in solution and can flocculate and form undesirable sediment in thebeverage.

To prevent sedimentation of the proteins when the mixture is added to abeverage, one or more pH buffer(s) may be added to the mixture so thatwhen the mixture is added to an acidic environment (such as coffee ortea), the resulting combination does not have a pH that is near or belowthe isoelectric point of the protein, thereby preventing sedimentationof the protein. But, the buffer system also should not negatively alterthe flavor profile of the protein paste and water mixture. Finding a pHbuffer that is soluble in the protein paste and water mixtures, does notnegatively affect the flavor profile of the protein paste and watermixture, and provides the pH buffering necessary to alter the pH of anacid environment so that the acidic environment does not have a pH nearor below the isoelectric point of the proteins, is a difficult task. Itwas found that some traditional food-grade pH buffers, such asphosphate-based pH buffers, do not provide the required buffering, andflocculation and sedimentation still occurred when using thephosphate-based buffers. Further, other buffers, such as calciumcarbonate, are not very soluble in the protein paste and water mixtureand cannot be added to the mixture in large enough amounts to providethe necessary buffering. To balance these considerations, inembodiments, a protein product comprises protein paste, water, sodiumbicarbonate (NaHCO₃), calcium carbonate (CaCO₃), and a stabilizer.

It was found that sodium bicarbonate increases the pH of the proteinpaste and water mixture. Sodium bicarbonate is highly soluble in waterand can be added to the mixture in large quantities. However, adding toomuch sodium bicarbonate to the mixture can lead to a noticeable metallictaste. In embodiments, sodium bicarbonate is included in the proteinpaste and water mixture in an amount greater than or equal to about 0.10wt. % of the mixture and less than or equal to about 0.50 wt. % of themixture, such as greater than or equal to about 0.20 wt. % of themixture and less than or equal to about 0.40 wt. % of the mixture. Inother embodiments, sodium bicarbonate is included in the protein pasteand water mixture in an amount greater than or equal to about 0.10 wt. %of the mixture and less than or equal to about 0.25 wt. % of themixture. In still other embodiments, sodium bicarbonate is included inthe protein paste and water mixture in an amount greater than or equalto about 0.25 wt. % of the protein product and less than or equal toabout 0.50 wt. % of the mixture, such as greater than or equal to about0.30 wt. % of the mixture and less than or equal to about 0.45 wt. % ofthe mixture.

As stated above, sodium bicarbonate is a useful buffer because, in part,sodium bicarbonate is highly soluble in water. However, when sodiumbicarbonate is used as the only buffer in the protein paste and watermixture, the amount of sodium bicarbonate required to provide thenecessary buffering causes the mixture to have a metallic flavor.Accordingly, in embodiments, calcium carbonate is added to the proteinproduct to provide additional buffering. As mentioned above, althoughcalcium carbonate is a strong buffer, it is not very soluble in waterand will precipitate out of solution if too much is added to the proteinpaste and water mixture. In embodiments, calcium carbonate is includedin the protein paste and water mixture in an amount greater than orequal to about 0.30 wt. % and less than or equal to about 0.80 wt. % ofthe mixture, such as greater than or equal to about 0.40 wt. % of themixture and less than or equal to about 0.70 wt. % of the mixture. Inother embodiments, calcium carbonate is included in the protein pasteand water mixture in an amount greater than or equal to about 0.30 wt. %of the mixture and less than or equal to about 0.60 wt. % of themixture, such as greater than or equal to about 0.35 wt. % and less thanor equal to about 0.55 wt. % of the mixture.

According to embodiments, the ratio of sodium bicarbonate and calciumcarbonate in the mixture is balanced to provide the desired amount ofbuffering and solubility. If the ratio of sodium bicarbonate to calciumcarbonate is too high, the amount of buffering will not be adequate tomaintain the pH of a solution comprising the mixture and a low-pHbeverage (such as, for example, coffee or tea) above the isoelectricpoint of the proteins. However, if the ratio of sodium bicarbonate tocalcium carbonate is too low, the buffers, such as calcium carbonate,will not be soluble in the mixture. Accordingly, in embodiments, theratio of sodium bicarbonate to calcium carbonate in the mixture is fromgreater than or equal to about 1.00:1.60 to less than or equal to about1.00:2.60, such as from greater than or equal to about 1.00:1.80 to lessthan or equal to about 1.00:2.40. In other embodiments, the ratio ofsodium bicarbonate to calcium carbonate in the mixture is from greaterthan or equal to about 1.00:1.90 to less than or equal to about1.00:2.30, such as from greater than or equal to about 1.00:2.00 to lessthan or equal to about 1.00:2.10.

The pH buffer system may be added to the protein product to raise the pHof the mixture so that when the mixture is added to an acidicenvironment, the pH of the composition is above the isoelectric point ofthe proteins in the mixture. In embodiments, the pH of the mixturecomprising the pH buffers is from greater than or equal to about 7.60 toless than or equal to about 8.40, such as from greater than or equal toabout 7.70 to less than or equal to about 8.30. In other embodiments,the pH of the mixture comprising the pH buffers is from greater than orequal to about 7.80 to less than or equal to about 8.20, such as fromgreater than or equal to about 7.90 to less than or equal to about 8.10.In way of contrast, and as an example only, the isoelectric point of theproteins in the mixture is from about 6.0 to about 6.4, such as about6.2.

Accordingly, it should be understood that embodiments of the mixture ofthe protein paste and water (i.e., the protein product) may comprise pHbuffers, including, without limitation, when the protein product isformulated for use as an enhancer for acidic beverages such as coffee ortea. However, it should be understood that these buffers are optionaland that, in some embodiments, the protein product may be formulatedwithout pH buffers.

In embodiments, stabilizers, such as starches and/or gums are added tothe mixture to promote the suspension of particulates, particularly thesuspension of protein particulates, in the water. Stabilizers may beadded to mixtures that are formulated with pH buffers and without pHbuffers. Suitable gum stabilizers include, without limitation, one ormore of xanthan gum, cellulose gum, cellulose gel, and carageenan gum.Suitable starch stabilizers include, without limitation, corn starch,tapioca starch, potato starch, and other similar starches. If too littlestabilizer is added to the mixture, the protein solids may fall out ofsuspension. However, if too much stabilizer is added to the mixture, thestabilizer may introduce off-notes in the protein product and/or maycause the stabilizer to form a gel in the mixture, both of which areundesirable. In embodiments, the stabilizer is included in the mixturein an amount greater than or equal to about 0.10 wt. % of the mixtureand less than or equal to about 0.80 wt. % of the mixture, such asgreater than or equal to about 0.20 wt. % of the mixture and less thanor equal to about 0.60 wt. % of the mixture. In other embodiments, thestabilizer is included in the mixture in an amount greater than or equalto about 0.30 wt. % of the mixture and less than or equal to about 0.50wt. % of the mixture, such as greater than or equal to about 0.35 wt. %of the mixture and less than or equal to about 0.45 wt. % of themixture. In some embodiments, the stabilizer comprises cellulose gum andcellulose gel gum greater than or equal to about 0.05 wt. % of themixture and less than or equal to about 0.20 wt. % of the mixture, suchas greater than or equal to about 0.10 wt. % of the mixture and lessthan or equal to about 0.15 wt. % of the mixture.

In embodiments, the mixture contains greater than or equal to about 0.5wt. % and less than or equal to about 8 wt. % total protein by weight ofthe mixture. For example, in some embodiments, the protein product maycontain greater than or equal to about 0.5 wt. % and less than or equalto about 6 wt. % total protein by weight of the mixture. In still otherembodiments, the protein product may contain greater than or equal toabout 1.0 wt. % and less than or equal to about 5 wt. % total protein byweight of the mixture. In still other embodiments, the protein productmay contain greater than or equal to about 2.0 wt. % and less than orequal to about 4 wt. % total protein by weight of the mixture.

In embodiments, the mixture contains greater than or equal to about 1gram and less than or equal to about 20 grams of protein per 240 ml ofthe mixture. For example, the mixture may contain greater than or equalto about 5 grams and less than or equal to about 20 grams of protein per240 ml of the mixture. In embodiments, the mixture contains greater thanor equal to about 1 gram or even 5 grams and less than or equal to about15 grams of protein per 240 ml of the mixture. In other embodiments, themixture contains greater than or equal to about 6 grams and less than orequal to about 10 grams of protein per 240 ml of the mixture or evengreater than or equal to about 7 grams and less than or equal to about10 grams of protein per 240 ml of the mixture. In still otherembodiments, the mixture contains greater than or equal to about 8 gramsand less than or equal to 10 grams of protein per 240 ml of the mixture.

The size of the particulate matter comprising protein in the mixture isdictated by the grinding and optional filtering steps describedhereinabove.

In the embodiments described herein, the mixture of protein paste andwater includes greater than or equal to about 40 wt. % and less than orequal to about 98 wt. % water. For example, in some embodiments, themixture of protein paste and water includes greater than or equal toabout 50 wt. % and less than or equal to about 95 wt. % water. In someother embodiments, the mixture of protein paste and water includesgreater than or equal to about 55 wt. % and less than or equal to about95 wt. % water. In some other embodiments, the mixture of protein pasteand water includes greater than or equal to about 60 wt. % and less thanor equal to about 90 wt. % water. In still other embodiments, themixture of protein paste and water includes greater than or equal toabout 65 wt. % and less than or equal to about 85 wt. % water. In stillother embodiments, the mixture of protein paste and water includesgreater than or equal to about 70 wt. % and less than or equal to about85 wt. % water.

As noted hereinabove the consistency of the mixture (and therefore theconsistency of the protein product) can be controlled by adjusting thepercentage of water in the mixture. For example, decreasing the watercontent may thicken the mixture, providing a protein product having theconsistency of a “smoothie” or a “shake.” However, increasing the watercontent may thin the mixture, providing a protein product having aconsistency more akin to dairy milk.

Adjusting the water content in the mixture also adjusts the viscosity ofthe mixture. In the embodiments described herein the mixture of proteinpaste and water in the protein product has a viscosity greater than orequal to about 15 centipoise (cP) and less than or equal to about 250cP. In embodiments, the viscosity of the mixture of protein paste andwater is greater than or equal to about 15 cP and less than or equal toabout 200 cP. In some embodiments, the mixture of the protein paste andwater in the protein product has a viscosity greater than or equal toabout 20 cP and less than or equal to about 150 cP. In some otherembodiments, the mixture of the protein paste and water in the proteinproduct has a viscosity greater than or equal to about 20 cP and lessthan or equal to about 50 cP.

In embodiments, a sweetener may be optionally added to the mixture ofprotein paste and water to enhance flavor. In some embodiments, thesweetener may be sucrose derived from sugarcane, however, it should beunderstood that other natural and artificial sweeteners are contemplatedand possible. In embodiments, the sweetener may be added to the mixtureof protein paste and water in an amount greater than or equal to about 0wt. % to less than or equal to about 10 wt. %. In some otherembodiments, the sweetener may be added to the mixture of protein pasteand water in an amount greater than or equal to about 1 wt. % to lessthan or equal to about 9 wt. %. In still other embodiments, thesweetener may be added to the mixture of protein paste and water in anamount greater than or equal to about 2 wt. % to less than or equal toabout 8 wt. %. In yet other embodiments, the sweetener may be added tothe mixture of protein paste and water in an amount greater than orequal to about 3 wt. % to less than or equal to about 7 wt. %.

In embodiments, an anti-foaming agent may be optionally added to themixture of protein paste and water to reduce foaming during processingand thereafter. In some embodiments, the anti-foaming agent may be, forexample, mono-diglyceride(s), mineral oil-based emulsions or vegetableoil-based emulsions or even silicon-based emulsions, however, it shouldbe understood that other anti-foaming agents are contemplated andpossible. In embodiments, the anti-foaming agent, when present, may beadded to the mixture of protein paste and water in an amount fromgreater than or equal to about 0.0001 wt. % to less than or equal toabout 0.0008 wt. %. In some other embodiments, the anti-foaming agentmay be added to the mixture of protein paste and water in an amountgreater than or equal to about 0.0002 wt. % to less than or equal toabout 0.0007 wt. % or even about 0.0006 wt. %. In still otherembodiments, the anti-foaming agent may be added to the mixture ofprotein paste and water in an amount greater than or equal to about0.0003 wt. % to less than or equal to about 0.0005 wt. %.

In embodiments, one or more vitamins, minerals, and/or essential acidsmay be added to the mixture of protein paste and water. In embodiments,the one or more vitamins, minerals, and or essential acids may be avitamin blend such as, for example a blend of vitamins E, A, D, and B12.However, it should be understood that other vitamins, minerals, and/oressential acids are contemplated and possible. For example, the one ormore vitamins, minerals, and/or essential acids may include, withoutlimitation, zinc and/or magnesium, and essential amino acids such aslysine. In embodiments, the one or more vitamins and/or minerals, whenpresent, may be added to the mixture of protein paste and water in anamount greater than or equal to about 0.0005 wt. % to less than or equalto about 0.1 wt. %. In some other embodiments, the one or more vitaminsand/or minerals may be added to the mixture of protein paste and waterin an amount greater than or equal to about 0.01 wt. % to less than orequal to about 0.07 wt. % or even about 0.06 wt. %. In still otherembodiments, the one or more vitamins and/or minerals may be added tothe mixture of protein paste and water in an amount greater than orequal to about 0.015 wt. % to less than or equal to about 0.05 wt. %.

In embodiments, one or more flavorings, such as natural and/orartificial flavoring, may be optionally added to the mixture of proteinpaste and water to enhance flavor. In some embodiments, the flavoringsmay be, for example vanilla, chocolate, nut blends, dairy, fruitflavors, caramel mocha, and/or various combinations thereof. However, itshould be understood that other flavorings and combinations offlavorings are contemplated and possible. In embodiments, theflavorings, when present, may be added to the mixture of protein pasteand water in an amount greater than or equal to about 0.02 wt. % to lessthan or equal to about 2.0 wt. %. In some other embodiments, theflavorings may be added to the mixture of protein paste and water in anamount greater than or equal to about 0.03 wt. % to less than or equalto about 1.75 wt. % or even about 1.5 wt. %. In still other embodiments,the flavorings may be added to the mixture of protein paste and water inan amount greater than or equal to about 0.05 wt. % to less than orequal to about 1.5 wt. %. In yet other embodiments, the flavorings maybe added to the mixture of protein paste and water in an amount greaterthan or equal to about 0.1 wt. % to less than or equal to about 1.0 wt.%. In other embodiments, the flavorings may be added to the mixture ofprotein paste and water in an amount greater than or equal to about 0.2wt. % to less than or equal to about 1.0 wt. %.

In embodiments, the mixture of the protein paste and water in theprotein product contains less than or equal to about 3 wt. % oil and fatby weight of the mixture. For example, in some embodiments, the mixturemay contain greater than or equal to about 0.5 wt. % and less than orequal to about 3.0 wt. % oil and fat by weight of the mixture. In someother embodiments, the mixture may contain greater than or equal toabout 1.0 wt. % and less than or equal to about 2.0 wt. % oil and fat byweight of the mixture.

The embodiments described herein will be further clarified by thefollowing examples.

EXAMPLES Example 1

For this study, 17 peanut paste samples were prepared. The samples wereproduced from peanuts processed at the temperatures and times listed inTable 1. Table 1 also lists the heat load for each sample, calculated asdescribed hereinabove. One sample (Example 9) of peanut milk (obtainedfrom peanuts processed at 240° F. (115.56° C.), for 35 minutes) was alsoprepared and analyzed.

TABLE 1 Peanut processing conditions for volatile organic aroma compoundanalysis Processing Temp Processing Time Heat Load Sample (F.) (minutes)(Calculated) Comparative 70 0 1 Example A Comparative 240 10 2.783Example B Comparative 240 15 4.174 Example C Comparative 240 20 5.565Example D Example 1 240 35 9.739 Example 2 240 120 33.391 Example 3 26010 35.938 Example 4 260 15 53.907 Example 5 260 20 71.876 Example 6 28510 879.92 Example 7 285 15 1319.88 Example 8 285 20 1759.8 Comparative295 15 4743.4 Example E Comparative 300 10 5994.8 Example F Comparative305 5 11364 Example G Comparative 310 10 21544 Example H Comparative 31015 32317 Example I Example 9 240 35 9.739 (Peanut Milk)

For peanut paste samples, each sample was prepared using 30 grams ofpeanut paste prepared from peanuts processed under one of the conditionsspecified in Table 1. After processing under the specified temperaturefor the specified time, the peanuts were ground into a peanut paste. Foreach sample, 30 grams of peanut paste was transferred to a beakertogether with 70 mL of water. Samples were homogenized in anUltra-Turrax homogenizer for 90 seconds to homogenize the mixture ofpeanut paste and water. Afterwards, 2,3-dimethoxytoluene (Sigma-Aldrich)was added as an internal standard (10 μL of a 300 ppm solution) to get aconcentration of 0.1 μg of internal standard per gram of peanut paste.The samples were then homogenized again in the Ultra-Turrax for 60seconds. Finally, 5 grams of each sample was placed in individual 20 mLvials. PDMS Twisters (Gerstel, 10 mm length, 1 mm film thickness) wereimmersed in the solutions, and stirred at 600 rpm for 90 minutes. Thetwisters were then dried before the analysis using 50 mL/min flowinghelium at a temperature of 50° C. for 5 minutes.

Each sample was analyzed for the presence of medium chain aldehydes andpyrazines using gas chromatography-mass spectrometry. In particular,analyses were carried out using an Agilent 6890 gas chromatographcoupled with a 5975 mass spectrometer, with a Gerstel TDSAThermodesorption autosampler, a Gerstel TDS3 Thermal desorption system,and CTS2 Cryo trapping system. Briefly, the desorption of the twistersin the thermal desorption system was done in splitless mode with aninitial temperature of 50° C., and a rate of 60° C./min to 240° C., witha hold of 5 minutes. In the cooled injection system, the initialtemperature was set at −120° C., with an initial time of 0.20 min. Thetemperature was increased at 12° C./s to 240° C. and held at thistemperature for 8 min. To improve separation, the conditions of thecryogenic trapping system were set at −80° C. (initial time 0.9), andthe temperature increased at a rate of 20° C./s to 240° C. and held atthis temperature for 1 min. For the injector, solvent vent mode was used(vent time 0 min, vent flow 50 ml/min, purge flow 50 ml/min, purge time0.70).

The separation was carried out using a VF-WAXMS column from Agilent (30m×0.25 mm×0.25 um), with an initial flow of 1.2 mL/min. The temperatureof the oven was programmed as follows: initial temperature 35° C. with ahold duration of 4 minutes; a first ramp at 3° C./min to 82° C.; and asecond ramp of 6° C./min to 220° C., and hold time of 10 min (total runtime: 53 min). Acquisition of the data was made in scan mode. Analysisof the samples was done in duplicate or triplicate.

The peanut milk sample was analyzed by placing 5 grams of peanut milk ina 20 mL vial with 23.8 μL of an internal standard solution (3 ppm inethanol). The sample consisted of 14% peanut paste and 86% water. Theamount of internal standard added was calculated to be the same finalconcentration (0.1 μg IS/g peanut paste) as in the peanut paste samplestaking into account that peanut milk was obtained using a proportion of1 gram peanuts/7 grams total of peanut milk.

After data collection by gas chromatography-mass spectrometry,chromatograms corresponding to the 17 peanut paste samples and thepeanut milk sample were analyzed using Chemstation (E.02.02, Agilent).Only those compounds with a mass spectra match factor in the NISTlibrary of 80% or higher were selected. In total, 60 compounds wereidentified, and for quantification, the main ion was used (Table 2).Results were expressed as relative areas (i.e., area of the main ioncompound/area of main ion Internal Standard).

TABLE 2 Compounds identified in peanut paste samples, their retentiontime (RT) in the chromatogram and the main ion used for quantificationpurposes. Ion RT Compound (m/z) 3.73 2-octene (Z) 70 4.27 Butanal,2-methyl 57 4.34 Butanal, 3-methyl 58 4.74 Benzene 78 5.043-cyclohepten-1-one 67 5.55 Pentanal 58 6.02 Decane 57 8.42 Hexanal*^(a)56 8.87 Undecane 57 10.13 3-penten-2-one, 4 methyl 83 11.52 Undecane,3-methyl 71 11.99 Pyridine 79 12.13 2-heptanone 58 12.27 Heptanal 7012.58 Limonene 68 12.92 Dodecane 57 13.51 2-hexenal (E)*^(a) 69 13.904-octanone 57 14.12 Furan, 2-pentyl 87 14.71 Nonadecane 85 15.261-pentanol 70 15.48 Pyrazine, methyl-*^(b) 94 16.42 2-octanone 58 16.61Octanal*^(a) 57 17.23 Tridecane 71 17.82 Pyrazine, 2,5-dimethyl*^(b) 10818.00 2-heptenal (E)*^(a) 83 18.35 Pyrazine, ethyl*^(b) 107 18.82Pyrazine, 2,3-dimethyl*^(b) 108 20.47 Pyrazine, 2-ethyl-6-methyl*^(b)121 20.70 Pyrazine, 2-ethyl-5-methyl*^(b) 121 20.81 2-nonanone 58 21.13Pyrazine, trimethyl*^(b) 122 21.20 Pyrazine, 2-ethyl, 3-methyl*^(b) 12121.41 3,5-octadien-2-ol 111 21.55 1,3-hexadiene,3-ethyl-2-methyl 6722.13 2-octenal (E)*^(a) 70 22.58 Pyrazine, 3-ethyl-2,5-dimethyl*^(b)135 23.02 Pyrazine, 2,5-diethyl*^(b) 121 23.07 Pyrazine,2,6-diethyl*^(b) 135 23.25 1-octen-3-ol 57 23.40 Furfural 96 23.94Pyrazine, 2-ethenyl, 6-methyl*^(b) 120 24.06 Pyrazine,3,5-diethyl-2-methyl*^(b) 149 24.10 2,4-heptadienal (E,E)*^(a) 81 24.182-decanone 58 24.63 3-nonen2-one 125 24.88 Benzaldehyde 77 25.242-nonenal*³ 70 25.26 Pyrazine, 2-methyl-3-(2-propenyl)*^(b) 133 26.16Pyridine, 2-hexyl 93 23.37 Pyridine, 3-methoxy 109 27.87Benzeneacetaldehyde 91 28.12 2,3-dimethoxytoluene (Internal Standard)152 29.09 2,4-nonadienal (E,E)*^(a) 81 30.13 2-undecenal 70 30.412,4-decadienal (E,E)*^(a) 81 31.28 2,4-decadienal (E,Z)*^(a) 81 37.832-methoxy-4-vinylphenol 150 39.18 Pyridine, 4-propyl 93 *Compoundsselected to obtain the ratio medium chain aldehydes (C6-C10)/totalpyrazines: ^(a)aldehydes; and ^(b)pyrazines

Principal Component Analysis (PCA) was applied to the data from thevolatile analysis to examine the relationship between the volatilecompounds and the roasting conditions of the peanut pastes (PCA done viaJMP software 11.1.1). In addition, a ratio of medium chainaldehydes/pyrazines was obtained for each sample by summing the relativeareas of all medium chain aldehydes (C6-C10) and dividing that sum bythe sum of the relative areas of all pyrazines. The aldehydes andpyrazines considered in this ratio are specified in Table 2. Table 3below contains the ratio of medium chain aldehydes to pyrazines for eachof the samples analyzed.

TABLE 3 Ratio of medium chain aldehydes:pyrazines for samples processedunder different conditions. Sample Ratio Comparative 632.9094 Example AComparative 272.2762 Example B Comparative 111.408 Example C Comparative48.62012 Example D Example 1 15.70111 Example 2 2.192143 Example 334.12674 Example 4 13.92974 Example 5 9.590366 Example 6 7.27839 Example7 3.459992 Example 8 2.280373 Comparative 0.900372 Example E Comparative1.452025 Example F Comparative 2.819362 Example G Comparative 0.820983Example H Comparative 0.418785 Example I Example 9 19.88 (Peanut Milk)

Referring now to FIGS. 3 and 4, FIG. 3 graphically depicts the ratio ofmedium chain aldehydes to pyrazines as a function of heat load and FIG.4 graphically depicts the ratio of medium chain aldehydes to pyrazinesas a function of processing conditions (i.e., time and temperature). Asshown in FIG. 3, the ratio of medium chain aldehydes to pyrazinesincreases exponentially with decreasing heat load and vice-versa. Thatis, the ratio of medium chain aldehydes to pyrazines decreasesexponentially with increasing heat load. FIG. 4 generally shows the sametrends with respect to combinations of temperature and time. It isbelieved that the discontinuity in FIG. 3 is due to the wider range oftimes tested at a temperature of 240° F. (115.6° C.) (10-120 minutes for240° F. compared to 10-20 minutes for other temperatures).

It is believed that these trends are due to the evolution of differentvolatile compounds at different heat loads achieved through differentprocessing conditions. Referring to FIGS. 5-7 by way of example, therelative amounts of the medium chain aldehyde hexanal (FIG. 5), thepyrazine compound methylpyrazine (FIG. 6), and the pyrazine compoundtrimethylpyrazine (FIG. 7) are graphically depicted as a function ofprocessing conditions. As shown in FIG. 5, it has been found thatgreater amounts of the medium chain aldehyde hexanal is produced atrelatively lower heat loads (i.e., combinations of lower temperaturesand/or processing times) which has the result of imparting a strong“grassy” or “beany” flavor to the finished product which may beundesirable. In contrast, it has also been found that the pyrazinecompounds, such as methylpyrazine and trimethylpyrazine, are produced atrelatively higher heat loads (i.e., combinations of higher temperaturesand/or processing times), as shown in FIGS. 6 and 7, which has theresult of imparting a strong “roasted” or even “burnt” flavor to thefinished product which may be undesirable. Based on this data, it hasbeen found that the roasted/burnt flavors due to pyrazines and thegrassy/beany flavors due to medium chain aldehydes can be reduced bycontrolling the heat load applied to the peanuts during processing,resulting in a finished product with a flavor profile acceptable toconsumers.

Example 2

To assess the effect of roasting time and temperature on proteinproducts comprising a mixture of protein particulates from peanuts andwater, peanuts were heated under three separate processing conditions:238° F. (114.4° C.) for 20 minutes corresponding to a heat load of4.308; 248° F. (120° C.) for 35 minutes corresponding to a heat load of27.01; and 255° F. (123.9° C.) for 35 minutes corresponding to a heatload of 1759. The protein products heated at 238° F. (114.4° C.) for 20minutes included 13.90 wt. % peanut paste; 85.10 wt. % water; 0.25 wt. %baking soda; 0.30 wt. % calcium carbonate; 0.40 wt. % cellulose gel, and0.05 wt. % carageenan. The protein products heated at 248° F. (120° C.)for 35 minutes included 8.68 wt. % peanut paste; 90.37 wt. % water; 0.25wt. % baking soda; 0.30 wt. % calcium carbonate; and 0.40 wt. %cellulose gel. The protein products heated at 255° F. (123.9° C.) for 35minutes included 11.81 wt. % peanut paste; 87.19 wt. % water; 0.25 wt. %baking soda; 0.30 wt. % calcium carbonate; 0.40 wt. % cellulose gel, and0.05 wt. % carageenan. The processed peanuts were then ground to form apeanut paste and approximately 14 grams of peanut paste were combinedwith approximately 86 mL of water and various additives and homogenizedto form a peanut milk product.

Thereafter, 2 samples of each peanut milk product were analyzed by gaschromatography-mass spectrometry to determine the ratio of medium chainaldehydes to pyrazines using the methods described in Example 1. It wasdetermined that the peanuts processed at 238° F. (114.4° C.) for 20minutes produced a peanut milk product having a ratio of medium chainaldehydes to pyrazines of 38.3 and 43.9, respectively. It was alsodetermined that the peanuts processed at 248° F. (120° C.) for 35minutes produced a peanut milk product having a ratio of medium chainaldehydes to pyrazines of 5.2 and 5.1, respectively. Finally, it wasdetermined that the peanuts processed at 255° F. (123.9° C.) for 35minutes produced a peanut milk product having a ratio of medium chainaldehydes to pyrazines of 1.6 and 1.7. This data generally indicatesthat relatively small increases in the time and temperature can have asignificant impact in decreasing the ratio of medium chain aldehydes topyrazines which, in turn, affects the flavor profile of the resultingpeanut milk product.

Example 3

In order to evaluate the effect of different sterilization processes onthe aggregation of protein in the peanut milk, four identical samples ofpeanut milk (Examples S1-S4) were prepared and processed under differentsterilization conditions. Each sample of peanut milk included 13.90 wt.% peanut paste; 84.7 wt. % water; 0.3 wt. % baking soda; 0.6 wt. %calcium carbonate; and 0.5 wt. % cellulose gel/cellulose gum. The peanutpaste was derived from peanuts initially steamed at 200° F. (93.33° C.)for 4.5 minutes and then heated at 270° F. for 35 minutes. The peanutswere then ground to a paste having an average particles size ofapproximately 39 microns. Example S1 was not subjected to asterilization process. Example S2 was subjected to a directsterilization process with the peanut milk being held at a temperatureof 275° F. for 7 seconds (the direct sterilization process will bedescribed in more detail below). Example S3 was subjected to an indirecttube and shell sterilization process, as depicted in FIG. 1, in whichthe peanut milk was held at a temperature of 275° F. for 7 seconds inthe tubular heater. Example S4 was subjected to an indirect scrapesurface sterilization process in which the peanut milk was held at atemperature of 275° F. for 7 seconds in the scrape surface heatexchanger.

The direct sterilization process to which Example S2 was subjectedincluded pre-heating the peanut milk in a plate-frame heat exchanger toa temperature of about 185° F. (85° C.) and, thereafter, directlyinjecting steam into the peanut milk (i.e., co-mingling the heatingutility (steam) with the peanut milk) to further heat the peanut milk to275° F. (135° C.). The peanut milk was held at this temperature for aperiod of seven seconds. The peanut milk was then passed into a vacuumchamber and subjected to a vacuum of −7 psi to extract the steamcondensate from the peanut milk. Thereafter, the peanut milk washomogenized at a temperature of 185° F. (85° C.) at a pressure of 3500psi. The peanut milk was then cooled in a tubular cooler to atemperature of 45° F. (7.2° C.).

Each of the samples was then analyzed with a light microscope todetermine the degree of protein aggregation which occurred in thesamples as well as the average aggregate size of the protein aggregates.The average aggregate size of the protein aggregates was determined byplacing a peanut milk sample on a microscope slide and a drop of acidfuchsin staining solution (0.1% w/w) was added. The acid fuchsinsolution stained the protein in the sample pink such that the proteinagglomerates could be visibly distinguished from the balance of thesample. Each slide was observed with an Axiophot Zeiss Upright lightmicroscope equipped with a Leica DFC425C CCD camera. Image-Pro® Plus 7.0software was used to capture images of each sample at a 10×magnification using the differential image contrast (DIC) opticalsetting. FIGS. 8-11 are magnified images of each of the samples showingthe degree of protein aggregation. The collected images were colorsegmented based on a histogram and then converted to black and white.The “Diameter” size measurement was selected in the Image-Pro® Plus 7.0software and “Apply Count/Measure” functions were used to detect allvisible bright (i.e., white) objects (i.e., protein agglomerates) in thefield and determine the size of each object and the average size of allthe objects detected.

More specifically, FIG. 8 is a magnified image of Example S1 which showsthat the peanut milk sample, without further processing, was fluid(relatively low viscosity) with well dispersed protein aggregatesthroughout. Image analysis of Example S1 indicated that the averageprotein aggregate size in the sample was 1.4 microns. It was alsodetermined that Example S1 had a viscosity of 11.4 centipoise (cP).

FIG. 9 is a magnified image of Example S2 which shows that the peanutmilk sample, after exposure to the direct sterilization process, wasfluid (relatively low viscosity) with well dispersed protein aggregatesthroughout. Image analysis of Example S2 indicated that the averageprotein aggregate size in the sample was 1.6 microns. It was alsodetermined that Example S2 had a viscosity of 14.9 (cP). Accordingly,Example S2 exhibited similar physical properties (protein aggregate sizeand viscosity) as Example S2 indicating that the direct sterilizationprocess did not cause significant aggregation of the proteins. It wasalso observed that, after the direct sterilization process, the peanutmilk of Example S2 had an obviously different color than Example S1, thecolor of Example S2 being more yellow than Example S1. While not wishingto be bound by theory, it is believed that this change in color may be aresult of the reduction/caramelization of sugar in the peanut milk as aresult of the direct sterilization process.

In addition to the average protein aggregate size and the viscosity,samples of the peanut milk of Example S2 were also analyzed to determinethe ratio of the total concentration of medium chain aldehydes in themixture to a total concentration of pyrazines in the mixture afterExample S2 was subjected to the direct sterilization process.Specifically, a sample of the peanut milk of Example S2 was analyzed intriplicate using the gas chromatography-mass spectrometry technique ofExample 1, described hereinabove. Based on this technique it wasdetermined that the average ratio of the total concentration of mediumchain aldehydes to the total concentration of pyrazines of the sample ofExample S2 was 0.7.

FIG. 10 is a magnified image of Example S3 which shows that the peanutmilk sample, after indirect sterilization, formed a loose, gel-like,non-dense network of relatively large protein aggregates. Image analysisof Example S3 indicated that the average protein aggregate size in thesample was 12 microns. It was also determined that Example S3 had aviscosity of 53.3 cP. It was also observed that, after indirectsterilization, the color of Example S3 did not change significantly fromthat of Example S1. While not wishing to be bound by theory, it isbelieved that the lack of a change in color may be a result of lessreduced/caramelized sugar in the peanut milk relative to Example S2which was subjected to the direct sterilization process. Thus, the dataderived from Example S3 indicates that different sterilizationtechniques may yield peanut milk products with different properties.

In addition to the average protein aggregate size and the viscosity,samples of the peanut milk of Example S3 were also analyzed to determinethe ratio of the total concentration of medium chain aldehydes in themixture to a total concentration of pyrazines in the mixture afterExample S3 was subjected to the indirect sterilization process.Specifically, a sample of the peanut milk of Example S3 was analyzed intriplicate using the gas chromatography-mass spectrometry technique ofExample 1, described hereinabove. Based on this technique it wasdetermined that the average ratio of the total concentration of mediumchain aldehydes to the total concentration of pyrazines of the sample ofExample S3 was 3.77.

FIG. 11 is a magnified image of Example S4 which shows that the peanutmilk sample, after indirect sterilization, formed a very loose,gel-like, non-dense network of relatively large protein aggregates.Image analysis of Example S4 indicated that the average proteinaggregate size in the sample was 6.4 microns. It was also determinedthat Example S4 had a viscosity of 14.9 cP. It was also observed that,after indirect sterilization, the color of Example S4 did not changesignificantly from that of Examples S1 and S3. Accordingly, like thedata derived from Example S3, the data derived from Example S4 indicatesthat different sterilization techniques may yield peanut milk productswith different properties.

In addition to the average protein aggregate size and the viscosity,samples of the peanut milk of Example S4 were also analyzed to determinethe ratio of the total concentration of medium chain aldehydes in themixture to a total concentration of pyrazines in the mixture afterExample S4 was subjected to the indirect sterilization process.Specifically, a sample of the peanut milk of Example S4 was analyzed intriplicate using the gas chromatography-mass spectrometry technique ofExample 1, described hereinabove. Based on this technique it wasdetermined that the average ratio of the total concentration of mediumchain aldehydes to the total concentration of pyrazines of the sample ofExample S4 was 6.29.

Example 4

In this study, 16 samples of protein products were prepared. Each samplestarted with a mixture of 14% protein paste and 86% water. The proteinpaste was prepared by heating shelled peanuts at 285° F. for 35 minutesand then grinding the peanuts into a paste. The paste was added to waterat 165° F. The mixture was then processed to remove insoluble solids andreduce fat. The resulting mixture was sterilized at 273° F. for 7seconds. 100 ml aliquots were used for testing. The buffers and/orstabilizers were added to the 100 ml aliquots, mixed with a handblender,and allowed to sit for 20 minutes. Of the samples, 11 samples were madewith sodium bicarbonate as the pH buffer and carageenan as thestabilizer. The remaining 5 samples used a mixture of calcium carbonateand sodium bicarbonate as the pH buffer and used carageenan as thestabilizer. The type and amount of pH buffers and stabilizers added tothe mixture of protein paste and water is shown in Table 4 below.

TABLE 4 Type and amounts of pH buffer and/or stabilizer. CarageenanSodium Bicarbonate Calcium Carbonate Sample (wt. %) (wt. %) (wt. %)Example 10 0.100 0.250 0.450 Example 11 0.100 0.375 0.450 Example 120.100 0.500 0.450 Comparative 0.000 0.250 0.000 Example J Comparative0.100 0.150 0.000 Example K Comparative 0.100 0.250 0.000 Example LComparative 0.100 0.375 0.000 Example M Comparative 0.200 0.250 0.000Example N Comparative 0.000 1.000 0.000 Example O Comparative 0.0000.500 0.000 Example P Comparative 0.050 0.250 0.000 Example QComparative 0.100 0.500 0.000 Example R Comparative 0.200 0.375 0.000Example S Comparative 0.200 0.375 0.000 Example T Comparative 0.1000.000 0.450 Example U Comparative 0.100 0.125 0.450 Example V

Once the pH buffer and stabilizer were added to the protein paste andwater mixture to form a buffered protein product, the pH of the proteinproduct was measured using a calibrated pH probe, and the flavor profileof the protein product was measured. Subsequently, 9 mL of the bufferedprotein product was added to 100 mL of coffee and stirred until theprotein product and coffee composition had a uniform color. The coffeewas prepared using a drip coffee brewer using one tablespoon of mediumroast coffee and 8 ounces of water. 100 ml aliquots of the coffeemixtures were measured and 9 ml of the protein mixture was added. Thestability of the protein product and coffee composition was visuallyinspected for sedimentation over a 15 minute period. A sample with nosedimentation was assigned a “yes” designation; a sample with anysedimentation was assigned a “no” designation. Results of this testingfor each sample are shown in Table 5 below.

TABLE 5 pH and flavor profile of buffered protein product and stabilityof coffee and protein product mixture. pH of Protein Acceptable FlavorAcceptable Sample Product Profile Stability Example 10 8.08 Yes YesExample 11 8.19 Yes Yes Example 12 8.31 Yes Yes Comparative 7.88 Yes NoExample J Comparative 7.46 Yes No Example K Comparative 7.80 Yes NoExample L Comparative 8.02 Yes No Example M Comparative 7.76 Yes NoExample N Comparative 8.10 No Yes Example O Comparative 7.94 No YesExample P Comparative 7.79 No Yes Example Q Comparative 8.18 No YesExample R Comparative 8.01 No Yes Example S Comparative 8.15 No YesExample T Comparative 7.52 Yes No Example U Comparative 7.76 Yes NoExample V

This data generally indicates that to achieve a protein product with anacceptable flavor profile and acceptable stability when the proteinproduct is added to coffee, a combination of sodium bicarbonate, calciumcarbonate, and stabilizer is required.

Based on the foregoing, it should be understood that the proteinproducts described herein comprise a mixture of water and particulatematter comprising protein derived from plants such as, for example andwithout limitation, tree nuts and/or legumes. The mixture has arelatively high concentration of total protein and, as such, is asuitable substitute for dairy milk. However, unlike dairy milk, theprotein product has relatively low cholesterol and is relatively low incalories. Moreover, the protein source is processed to minimize ormitigate the impact of volatile organic aroma compounds on the flavor ofthe protein product. For example, in embodiments, the ratio of the totalconcentration of medium chain aldehydes in the water and particulatematter mixture to the total concentration of pyrazines in the water andparticulate matter mixture is greater than or equal to 0.5 and less thanor equal to 45 to minimize or mitigate off flavors imparted to theprotein product by the protein source. In some embodiments, the mixtureis sterilized using indirect sterilization processes to yield asterilized mixture which comprises protein aggregates having an averageaggregate size of greater than or equal to 4 microns with a loose,gel-like, non-dense structure which may improve the perceived textureand mouth feel of the mixture. In some embodiments, the protein productcomprises buffers that provide stability when the protein product isadded to an acidic environment.

It will be apparent to those skilled in the art that variousmodifications and variations can be made to the embodiments describedherein without departing from the spirit and scope of the claimedsubject matter. Thus it is intended that the specification cover themodifications and variations of the various embodiments described hereinprovided such modification and variations come within the scope of theappended claims and their equivalents.

1-30. (canceled)
 31. A protein product comprising: a mixture of waterand particulate matter comprising protein, the mixture comprising:medium chain aldehydes and pyrazines, wherein a ratio of a totalconcentration of medium chain aldehydes in the mixture to a totalconcentration of pyrazines in the mixture, as determined by gaschromatography-mass spectrometry, is greater than or equal to 0.5 andless than or equal to 20; from about 1.0 wt. % to about 5.0 wt. % totalprotein by weight of the mixture; from about 40 wt. % to about 98 wt. %water by weight of the mixture; less than or equal to about 4.0 wt. %oil and fat by weight of the mixture; and greater than or equal to about0 wt. % to less than or equal to about 10 wt. % sweetener, wherein theparticulate matter has an average particle size less than or equal toabout 50 μm.
 32. The protein product of claim 31, wherein theparticulate matter comprising protein is derived from at least one oftree nuts and peanuts.
 33. The protein product of claim 31, wherein theaverage particle size of the particulate matter comprising protein isless than or equal to about 45 μm.
 34. The protein product of claim 31,wherein the ratio of the total concentration of medium chain aldehydesin the mixture to the total concentration of pyrazines in the mixture,as determined by gas chromatography-mass spectrometry, is greater thanor equal to 0.75 and less than or equal to
 10. 35. The protein productof claim 31, wherein the ratio of the total concentration of mediumchain aldehydes in the mixture to the total concentration of pyrazinesin the mixture, as determined by gas chromatography-mass spectrometry,is greater than or equal to 1 and less than or equal to
 5. 36. Theprotein product of claim 31, wherein the mixture comprises from about2.0 wt. % to about 4 wt. % total protein by weight of the mixture. 37.The protein product of claim 31, wherein the mixture comprises fromabout 70 wt. % to about 85 wt. % water by weight of the mixture.
 38. Theprotein product of claim 31, wherein the mixture comprises greater thanor equal to about 0.5 wt. % oil and fat by weight of the mixture. 39.The protein product of claim 31, wherein the mixture has a viscositygreater than or equal to about 15 cP and less than or equal to about 250cP.
 40. The protein product of claim 31, wherein the particulate mattercomprising protein is derived from peanuts and has an average aggregatesize of greater than or equal to 4 microns.
 41. A protein productcomprising: a mixture of water and particulate matter comprisingprotein, the mixture comprising: medium chain aldehydes and pyrazines,wherein a ratio of a total concentration of medium chain aldehydes inthe mixture to a total concentration of pyrazines in the mixture, asdetermined by gas chromatography-mass spectrometry, is greater than orequal to 0.5 and less than or equal to 45; from about 0.5 wt. % to about8.0 wt. % total protein by weight of the mixture; from about 40 wt. % toabout 98 wt. % water by weight of the mixture; and less than or equal toabout 4.0 wt. % oil and fat by weight of the mixture, wherein theparticulate matter comprising protein has an average particle size lessthan or equal to about 50 μm, the particulate matter comprising proteinis processed under a heat load greater than or equal to about 20 andless than or equal to about
 125. 42. The protein product of claim 41,wherein the particulate matter comprising protein is processed under aheat load greater than or equal to about 35 and less than or equal toabout
 50. 43. The protein product of claim 41, wherein the particulatematter comprising protein is derived from peanuts processed at aprocessing temperature greater than or equal to about 238° F. and lessthan or equal to about 310° F. for a processing time greater than orequal to about 10 minutes and less than or equal to about 120 minutes.44. The protein product of claim 41, wherein the particulate mattercomprising protein is derived from peanuts processed at a processingtemperature greater than or equal to about 280° F. and less than orequal to about 310° F. for a processing time greater than or equal toabout 15 minutes and less than or equal to about 35 minutes.
 45. Theprotein product of claim 41, wherein the mixture comprises from about0.5 wt. % to about 6 wt. % total protein by weight of the mixture. 46.The protein product of claim 41, wherein the mixture comprises fromabout 70 wt. % to about 85 wt. % water by weight of the mixture.
 47. Theprotein product of claim 41, wherein the particulate matter comprisesprotein aggregates having an average aggregate size of less than orequal to 144 microns.
 48. The protein product of claim 41, wherein themixture has a viscosity greater than or equal to about 15 cP and lessthan or equal to about 250 cP.
 49. A method of making a protein product,the method comprising: processing nuts at a heat load greater than orequal to about 20 and less than or equal to about 125, wherein the nutsare at least one of tree nuts and peanuts; grinding the nuts therebyforming a protein paste; blending the protein paste with water therebyforming a mixture having a total protein content from about 0.5 wt. % toabout 8.0 wt. % by weight of the mixture; reducing an oil and fatcontent of the mixture to less than or equal to about 4.0 wt. % byweight of the mixture; and sterilizing the mixture with an indirectsterilization process whereby, after sterilization, the mixturecomprises protein aggregates having an average aggregate size greaterthan or equal to 4 microns.
 50. The method of claim 49, wherein, aftersterilization, the mixture comprises protein aggregates having anaverage aggregate size less than or equal to 144 microns.
 51. The methodof claim 49, wherein the nuts are processed at a processing temperaturegreater than or equal to about 238° F. and less than or equal to about310° F. for a processing time greater than or equal to about 10 minutesand less than or equal to about 120 minutes.
 52. The method of claim 49,wherein the nuts are processed at a processing temperature greater thanor equal to about 280° F. and less than or equal to about 310° F. for aprocessing time greater than or equal to about 15 minutes and less thanor equal to about 35 minutes.
 53. The method of claim 49, wherein, afterprocessing, the nuts have a moisture content greater than or equal to 1wt. % and less than or equal to about 4 wt. % by weight of the mixture.54. The method of claim 49, wherein the heat load is greater than orequal to 35 and less than or equal to
 50. 55. The method of claim 49,wherein the protein paste comprises particulate matter comprisingprotein with an average particle size less than or equal to about 50 μm.56. The method of claim 49, wherein the protein paste is blended withwater in a ratio from about 1:5 to about 1:7.
 57. The method of claim49, wherein, after reducing, an oil and fat content of the mixture isgreater than about 0.5 wt. % by weight of the mixture.
 58. The method ofclaim 49, wherein the oil and fat content of the mixture is reduced byheating the mixture in a separator at a temperature from about 50° C. toabout 90° C.
 59. The method of claim 49, further comprising homogenizingthe mixture under pressure at elevated temperatures.
 60. The method ofclaim 59, wherein, after homogenizing, the mixture comprises mediumchain aldehydes and pyrazines and a ratio of a total concentration ofmedium chain aldehydes in the mixture to a total concentration ofpyrazines in the mixture, as determined by gas chromatography-massspectrometry, is greater than or equal to 0.75 and less than or equal to10.